Recombinant Thioredoxin

Recombinant E.Coli Thioredoxin produced in E.Coli contains a single disulfide active site and has a molecular mass of 11.9 kDa. The pI of the TRX is 4.67.

Description:

Thioredoxins are small disulphide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. This could be especially useful in refolding proteins expressed in E. coli. To this end, thioredoxin has been shown to act as a protein disulfide isomerase.